ID H1W561_COLHI Unreviewed; 1965 AA.
AC H1W561;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:CCF47625.1};
GN ORFNames=CH063_04219 {ECO:0000313|EMBL:CCF47625.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF47625.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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DR EMBL; CACQ02009945; CCF47625.1; -; Genomic_DNA.
DR STRING; 759273.H1W561; -.
DR EnsemblFungi; CCF47625; CCF47625; CH063_04219.
DR VEuPathDB; FungiDB:CH63R_10337; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1880..1957
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1965 AA; 214919 MW; EFCAF5BA5CC23878 CRC64;
MGKGLSAYKP FRDSVLRSEL VLKSLGCPWT LTEELERGEA DCNLRRTDYS QPACTALQVA
LVDLMKAWGV KPVAVVGHSS GEIAAAYCAG FIDHEAAVKI AWLRGQVSQT VSRNGGMLAV
SASAESVGEH LRSLKLGKAV VGCLNSPKAC TVSGDNMAIE ELQEILAEAQ IACTRLPMDV
AYHSFHMEAA RERYEAALKG IAHGSSDIPM FSSVSGKLVT AEQMTPSYWV DNLVSPVNFV
GAVRSLLHHT EGKARSHDRT AFASVFVELG PHSALRSYLL DTFATEDRFS DLSYATALRR
KFDGVQTALE AMGQLWAKGC EVDVNRVNEV SDSTGMLVDL PPYAWNHTRE FWDESYLSRE
YRLREKPRTD LLGYRMSGTP DPTWRCHLRC AESPWIREHK VQGDILYPGA GIVIMAIEAA
RQLAEEHDTE EIHGYELRDV AIDTALRVPD TEKGIEVMIQ LHARRTGTKA APSATLNEFS
VSSWSEEIRE WTVHARGLVS VTFKSALSPS MQRELALENE RYAQSFADAR KICQKPARSF
LYDTVETIGM QYGPTFRNMT ELFAGPNASY GVISVPDTKS VMPKGFEYPN VVHPATLDSV
LHLLFPSISG EDQSLSEAVV PFSFDRIFVS ARLSGVPGTR LHGCSTAQKT SYTTWKSSIT
ISEDLSEPMI VMEGVSLASV GEGDAQKTQE TRASCFGQTW HEDADLLEPS QVKELVYRRT
LKSKDDESVL DKLEYVCLVH IYRCLAWLGS DEGRAFVPQD GFWKLYVEWM RDTIKQFPPL
AGSEAEVEAE LDAARKRIVL SESGDITVQM VDRIGENLRR IFSREVEPLQ VMTEGDLLYS
FYRGAFGTSF NTNVAEYVGM VADKSPGVKI LEIGAGTGGT TYHVLERLRN PDGSSKAAKY
CFTDISPGFL AKAADRFSED ASIMEFTTLN IENEPAEQGF EPESYDLIVC ANVLHATKSI
QETLAHCRSL LKPGGRLVLS EVTIKRIFSG FIMGPLPGWW LGEDDGRKGG PLLDVDEWNT
ALVQAGFSGV DVDIRGDREV SREPVSLILS TKPEAQAPGP SQFVIVSTGS EASEKLSLSI
QKQLVSASQD VAVLQWNDLD DASNGQVEGK YCLCLAEWEN PVLSNLTDAD WERLRHVILR
SAGTLWITGG AAMECPEPMK SLMVGLSRAI RNENAGVRLA TLDLETPSTI DFDDAAKNVL
KVALSHSRGD GFDGEYAARG SVVYVPRVER TLGVDASLRK YEAKGQPELV SFKGCGRPLK
LTIKTPGLLD TFRWEEDEVY YEPLAEDWIE VEVKAVGLNF KDVLVALGNL AENKLGVDAS
GVVTRVGAAV SDFKPGDRVM TASCDTFATY VRFPAKGAIA VPETMTFEEA ASMPLIFLTA
QYSLVTAGNL VRGEKILIHA AAGGVGQAAI MIAQRKGAEI FATVGSDEKK QLIMDQYGIP
EDHIFSSRDA SFAKAVMRAT DGRGVDVVLN SLAGELLRVS WHCLAKFGRF LEIGKADLFA
NTGLDMKPFL DNKAYIGVNL LDFENNPTPR AVALWEDTAR LIHDGSVKPI APLQLFSMAE
VEKAFRYMQA GKHMGKVVVR VDDADMVPAV PRIPRVDIHA DATYVIAGVG GICKEIGRWL
AEKGARHLVL LSRSAASGEE NKAFAAELQK TFGAATYAYD CDVGNKTALG QVLDDLKSKD
VPEIKGCVTG AMVLRDTLFD AMTADHVRTT VGPKVHGTWN LHELLPKELD FFVMLSSLAG
VMGHRGQGNY GCGNIFQDYF AAYRRALGLR AMTVDIGYLL SVGFVAEHDE YVDHVKAMGL
KVMHKSDLHG LMATALEGSG AHPAQVMCGL PYNEHDDAWY WIQDQRFAGL RKKASGAGAG
GSASVSLRDE LVRXGKADGE AVDLITSALV QRLAKLMMMP EDDVDAGKPL SAYGVDSLVA
VEVRNWIAKE VAVEVSVFDI MANIPMRQLA ADLAGKSKLL VQEAS
//
